Research@StAndrews
 
The University of St Andrews

Research@StAndrews:FullText >
University of St Andrews Research >
University of St Andrews Research >
University of St Andrews Research >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10023/1027
This item has been viewed 1 times in the last year. View Statistics

Files in This Item:

File Description SizeFormat
White-BMCMolecularBiology2008-9.pdf721.62 kBAdobe PDFView/Open
Title: The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase and is recruited to DNA following gamma irradiation in the archaeon Sulfolobus acidocaldarius
Authors: Quaiser, Achim
Constantinesco, Florence
White, Malcolm F
Forterre, Patrick
Elie, Christiane
Keywords: Strand break repair
Hyperthermophilic archaeon
Homologous recombination
Pyrococcus-furiosus
Escherichia-coli
Thermophilic archaea
Ionizing-radiation
Chromosome segregation
Genetic-recombination
Replication forks
QH426 Genetics
Issue Date: 22-Feb-2008
Citation: Quaiser , A , Constantinesco , F , White , M F , Forterre , P & Elie , C 2008 , ' The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase and is recruited to DNA following gamma irradiation in the archaeon Sulfolobus acidocaldarius ' BMC Molecular Biology , vol 9 , 25 .
Abstract: Background: The ubiquitous Rad50 and Mre11 proteins play a key role in many processes involved in the maintenance of genome integrity in Bacteria and Eucarya, but their function in the Archaea is presently unknown. We showed previously that in most hyperthermophilic archaea, rad50-mre11 genes are linked to nurA encoding both a single-strand endonuclease and a 5' to 3' exonuclease, and herA, encoding a bipolar DNA helicase which suggests the involvement of the four proteins in common molecular pathway(s). Since genetic tools for hyperthermophilic archaea are just emerging, we utilized immuno-detection approaches to get the first in vivo data on the role(s) of these proteins in the hyperthermophilic crenarchaeon Sulfolobus acidocaldarius. Results: We first showed that S. acidocaldarius can repair DNA damage induced by high doses of gamma rays, and we performed a time course analysis of the total levels and sub-cellular partitioning of Rad50, Mre11, HerA and NurA along with the RadA recombinase in both control and irradiated cells. We found that during the exponential phase, all proteins are synthesized and display constant levels, but that all of them exhibit a different sub-cellular partitioning. Following gamma irradiation, both Mre11 and RadA are immediately recruited to DNA and remain DNA-bound in the course of DNA repair. Furthermore, we show by immuno-precipitation assays that Rad50, Mre11 and the HerA helicase interact altogether. Conclusion: Our analyses strongly support that in Sulfolobus acidocaldarius, the Mre11 protein and the RadA recombinase might play an active role in the repair of DNA damage introduced by gamma rays and/or may act as DNA damage sensors. Moreover, our results demonstrate the functional interaction between Mre11, Rad50 and the HerA helicase and suggest that each protein play different roles when acting on its own or in association with its partners. This report provides the first in vivo evidence supporting the implication of the Mre11 protein in DNA repair processes in the Archaea and showing its interaction with both Rad50 and the HerA bipolar helicase. Further studies on the functional interactions between these proteins, the NurA nuclease and the RadA recombinase, will allow us to define their roles and mechanism of action.
Version: Publisher PDF
Status: Peer reviewed
URI: http://hdl.handle.net/10023/1027
DOI: http://dx.doi.org/10.1186/1471-2199-9-25
ISSN: 1471-2199
Type: Journal article
Rights: This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Appears in Collections:University of St Andrews Research
Biology Research
Biomedical Sciences Research Complex (BSRC) Research



This item is protected by original copyright

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

DSpace Software Copyright © 2002-2012  Duraspace - Feedback
For help contact: Digital-Repository@st-andrews.ac.uk | Copyright for this page belongs to St Andrews University Library | Terms and Conditions (Cookies)